ArticleBiophysical journal2013
Investigation of homeodomain membrane translocation properties: insights from the structure determination of engrailed-2 homeodomain in aqueous and membrane-mimetic environments.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- A cationic motif upstream Engrailed2 homeodomain controls cell internalization through selective interaction with heparan sulfates.Nature communications · 2023Article
- Role of PI(4,5)P2 and Cholesterol in Unconventional Protein Secretion.Advances in experimental medicine and biology · 2023Article
- Designed Multifunctional Peptides for Intracellular Targets.Antibiotics (Basel, Switzerland) · 2022Review
- Homeoprotein transduction in neurodevelopment and physiopathology.Science advances · 2020Review
- Altered staining patterns and expression level of Engrailed-2 in benign prostatic hyperplasia and prostate Cancer predict prostatic disease progression.BMC cancer · 2020Observational
- Graftable SCoMPIs enable the labeling and X-ray fluorescence imaging of proteins.Chemical science · 2018Article
- Distribution of Pico- and Nanosecond Motions in Disordered Proteins from Nuclear Spin Relaxation.Biophysical journal · 2015Article
- The role of epigenetic-related codes in neurocomputation: dynamic hardware in the brain.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Life without glutamate: the epigenetic effects of glutamate deletion.Frontiers in molecular neuroscience · 2014Article
- Hypotheses concerning how Otx2 makes its incredible journey: a hitchhiker on the road to Rome?Frontiers in molecular neuroscience · 2013Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In addition to their well-known DNA-binding properties, homeodomains have the ability to efficiently translocate across biological membranes through still poorly-characterized mechanisms. To date, most biophysical studies addressing the mechanisms of internalization have focused on small synthetic peptides rather than full-length globular homeodomains. In this work, we characterized the conformational properties of chicken Engrailed 2 homeodomain (En2HD) in aqueous solution and in membrane mimetic environments using circular dichroism, Trp fluorescence, and NMR spectroscopy. En2HD adopts a well-defined three-helical bundle fold in aqueous solution. The Trp-48 residue, which is critical for internalization, is fully buried in the hydrophobic core. Circular dichroism and fluorescence reveal that a conformational transition occurs in anionic lipid vesicles and in micelles. En2HD loses its native three-dimensional structure in micellar environments but, remarkably, near-native helical secondary structures are maintained. Long-range interactions could be detected using site-directed spin labels, indicating that the three helices do not adopt extended orientations. Noncovalent paramagnetic probes yielded information about helix positioning and unveiled the burial of critical aromatic and basic residues within the micelles. Our results suggest that electrostatic interactions with membranes may be determinant in inducing a conformational change enabling Trp-48 to insert into membranes.
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